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@ARTICLE{Dee+06,
  author = {S. Deechongkit and H. Nguyen and M. Jager and E. T. Powers and M.
           Gruebele and J. W. Kelly},
  year = 2006,
  title = {Beta-Sheet Folding Mechanisms from Perturbation Energetics},
  journal = {Curr. Opin. Struct. Biol.},
  volume = 16,
  pages = {94--101}
}
@ARTICLE{BeCK05,
  author = {Robert B. Best and Jane Clarke and Martin Karplus},
  year = 2005,
  title = {What Contributions to Protein Side-Chain Dynamics are Probed by
          {NMR} Experiments? A Molecular Dynamics Simulation Analysis},
  journal = {J. Mol. Biol.},
  volume = 349,
  pages = {185--203}
}
@ARTICLE{Bou+05,
  author = {Guillaume Bouviginies and Pau Bernad{\'o} and Sebastian Meier and
           Kyuil Cho and Stephan Grzesiek and Rafael Br{\"u}schweiler and
           Martin Blackledge},
  year = 2005,
  title = {Identification of Slow Correlated Motions in Proteins Using
          Residual Dipolar and Hydrogen-Bond Scalar Couplings},
  journal = {PNAS},
  volume = 102,
  pages = {13885--13890}
}
@ARTICLE{NJKG05,
  author = {H. Nguyen and M. Jager and J. W. Kelly and M. Gruebele},
  year = 2005,
  title = {Engineering a Beta-Sheet Protein Toward the Folding Speed Limit},
  journal = {J. Phys. Chem. B},
  volume = 109,
  pages = {15182--15186},
  abstract = {Recent experimental studies have shown that a.-helical proteins
             can approach the folding "speed limit", where folding switches
             from an activated to a downhill process in free energy.
             beta-sheet proteins are generally thought to fold more slowly
             than helix bundles. However, based on studies of hairpins,
             folding should still be able to approach the microsecond time
             scale. Here we demonstrate how the hPin1 WW domain, a
             triple-stranded beta-sheet protein with a sharp thermodynamic
             melting transition, can be engineered toward the folding "speed
             limit" without a significant loss in thermal denaturation
             cooperativity.}
}
@ARTICLE{Ber+04,
  author = {Pau Bernad{\'o} and Miguel X. Fernandes and Doris M. Jacobs and
           Klaus Fiebig and Jos{\'e} Garc{\'{\i}}a de la Torre and Miquel Pons},
  year = 2004,
  title = {Interpretation of {NMR} Relaxation Properties of Pin1, a Two-Domain
          Protein, Based on {B}rownian Dynamic Simulations},
  journal = {J. of Biomolecular NMR},
  volume = 29,
  pages = {21--35}
}
@ARTICLE{KrDS04,
  author = {Bryan A. Krantz and Robin S. Dothager and Tobin R. Sosnick},
  year = 2004,
  title = {Discerning the Structure and Energy of {MultipleTransition} States
          in Protein Folding Using Psi-Analysis},
  journal = {J. Mol. Biol.},
  volume = 337,
  pages = {463--475},
  abstract = {We quantify the degree to which folding occurs along a complex
             landscape with structurally distinct pathways using c-analysis in
             combination with a protein engineering method that identifies
             native, non-covalent polypeptide interactions and their relative
             populations at the rate-limiting step. By probing the proximity
             of two specific partners, this method is extremely well-suited
             for comparison to theoretical simulations. Using ubiquitin as a
             model system, we detect individual pathways with siteresolved
             resolution, demonstrating that the protein folds through a
             native-like transition state ensemble with a common nucleus that
             contains heterogeneous features on its periphery. The consensus
             transition state topology has part of the major helix docked
             against four properly aligned b-strands. However, structural
             heterogeneity exists in the transition state ensemble, wherein
             peripheral regions are differentially populated according to
             their relative stability. Pathway diversity reflects the variable
             order of formation of these peripheral elements, which radiate
             outward from the common nucleus. These results, which show only
             moderate agreement with traditional mutational f-analysis,
             provide an extraordinarily detailed and quantitative description
             of protein folding.}
}
@ARTICLE{PrSB01,
  author = {J. J. Prompers and C. Scheurer and R. Br{\"u}schweiler},
  year = 2001,
  title = {Characterization of {NMR} Relaxation-Active Motions of a Partially
          Folded {A}-State Analogue of Ubiquitin},
  journal = {J. Mol. Biol.},
  volume = 305,
  pages = {1085--1097}
}
